|Other Names||E3 ubiquitin-protein ligase MARCH1, 632-, Membrane-associated RING finger protein 1, Membrane-associated RING-CH protein I, MARCH-I, RING finger protein 171, MARCH1, RNF171|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells, down-regulates their cell surface localization thus sequestering them in the intracellular endosomal system.|
|Cellular Location||Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein|
|Tissue Location||Expressed in antigen presenting cells, APCs, located in lymph nodes and spleen. Also expressed in lung Expression is high in follicular B-cells, moderate in dendritic cells and low in splenic T-cells.|
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Provided below are standard protocols that you may find useful for product applications.
MARCH1 is a member of the MARCH family of membrane-boundE3 ubiquitin ligases (EC 22.214.171.124). MARCH proteins add ubiquitin(see MIM 191339) to target lysines in substrate proteins, therebysignaling their vesicular transport between membrane compartments.MARCH1 downregulates the surface expression of majorhistocompatibility complex (MHC) class II molecules (see MIM142880) and other glycoproteins by directing them to the lateendosomal/lysosomal compartment (Bartee et al., 2004 [PubMed14722266]; Thibodeau et al., 2008 [PubMed 18389477]; De Gassart etal., 2008 [PubMed 18305173]).
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Thibodeau, J., et al. Eur. J. Immunol. 38(5):1225-1230(2008)De Gassart, A., et al. Proc. Natl. Acad. Sci. U.S.A. 105(9):3491-3496(2008)Bartee, E., et al. J. Virol. 78(3):1109-1120(2004)
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